G04SecL04Tpc1: Difference between revisions

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===Osp-B H6831 complex===

~~The complex formed by the C-terminal end of~~ Outer Surface Protein B ~~and H6831 displays~~ a <scene name='G04SecL04Tpc1/Osp_b_fab_complex/1'>truncated form of Osp-B</scene>, purple,~~Binding with~~ the Fab ~~region~~ of the H6831~~, light blue~~.

In its original form,Outer Surface Protein B has 12 Beta sheets. However, a <scene name='G04SecL04Tpc1/Osp_b_fab_complex/1'>truncated form of Osp-B</scene>, purple, is displayed in the complex formed when the C-terminus of Osp B binds to the antibody H6831. The Osp B binds to the Fab <scene name='G04SecL04Tpc1/L_chain/1'> light chain</scene> and <scene name='G04SecL04Tpc1/H_chain/1'>heavy chain</scene>regions of the H6831.

There are three loop regions on the c-terminal Osp-B that interact with the Fab of H6831. The major interactions of the complex occur between loop region two and the Fab heavy chain. More minor hydrogen bonding interactions occur between loop one and the heavy chain as well as loop three and the light chains

There are <scene name='G04SecL04Tpc1/Osp_b_fab_complex/8'>three loop regions</scene> on the c-terminal Osp-B that interact with the Fab of H6831. The major interactions of the complex occur between loop region two, seen in pink, and the Fab heavy chain. More minor hydrogen bonding interactions occur between loop one,green, and the heavy chain as well as loop three,orange, and the light chains

<ref name="Becker M">PMID:15713683</ref>. The essential residue on loop two is the <scene name='G04SecL04Tpc1/Osp_b_fab_complex/6'>Lysine 253</scene>shown in green. This lysine forms an ion pair with a <scene name='G04SecL04Tpc1/Osp_b_fab_complex/4'>Glutamic acid 50</scene>, red, of the Fab heavy chain. This antigen-antibody complex is further stabilized by the presence of a <scene name='G04SecL04Tpc1/Osp_b_fab_complex/5'>Threonine 276</scene>, orange. This bond is locked in by the presence of two

<scene name='G04SecL04Tpc1/Osp_b_fab_complex/7'>aromatic residues</scene> that reside on the Fab, tryptophan and tyrosine shown in black. There are some instances in which the H6831 cannot bind to Osp-B. This is a case of a mutant form of the protein in which the essential lysine is replaced by another residue<ref name="Becker M">PMID:15713683</ref>.

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Another surface protein of note in the B. Burgdorferi is <scene name='G04SecL04Tpc1/Ospa_complex/1'>OspA</scene>, ~~which is~~ 53% similar to OspB. ~~This~~ is ~~due to some structural similarities~~ in the ~~proteins~~. ***More contents will be done before noon.~~***~~

Another surface protein of note in the B. Burgdorferi is outer surface protein A <scene name='G04SecL04Tpc1/Ospa_complex/1'>OspA</scene>. It is composed of 21 anti-parallel beta-sheets and one alpha-helix. It contains a B-cell epitope on its C-terminal that binds with monoclonal antibody LA-2. LA-2 is a regular-structured antibody that is composed of two heavy chains and two light chains. <ref name="Ding,W">PMID: 11183781</ref>.

Complex proteins OspB and OspA are shown to be 53% similar due to structural similarities<ref name="Li,H">PMID: 9108020</ref>. The H6831 and LA-2 antibodies are also structurally similar, and each binds near the C-terminus on its respective surface protein. The H6831 and LA-2 epitopes on OspB and OspA are positioned at the opposite end of the molecule as the N-terminus of each antigen. On the C-terminal tips on each protein, the epitopes contain three exposed loops of residues that are involved with the binding interaction between antigen and antibody. For OspB, the middle loop (loop 2) has been shown to have the strongest interaction with H6831. The residue Lys253 in this loop is especially important in the interaction. For OspA, one of the outer loops (loop 1) has the strongest interaction with LA-2. The <scene name='G04SecL04Tpc1/Ospa_complex/6'>Alanine 208</scene> residue in the loop plays the important role here. The importance of these residues is confirmed by observing antibody reactivity using different species of Borrelia<ref name="Ding,W">PMID: 11183781</ref><ref name="Li,H">PMID: 9108020</ref>. Also, researchers found that buried surface area of OspA in LA-2 Fab is larger than OspB in the H6831Fab<ref name="Becker M">PMID:15713683</ref>).

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@@ Line 10: / Line 10: @@
 ===Osp-B H6831 complex===
-The complex formed by the C-terminal end of Outer Surface Protein B and H6831 displays a  <scene name='G04SecL04Tpc1/Osp_b_fab_complex/1'>truncated form of Osp-B</scene>, purple,Binding with the Fab region of the H6831, light blue.
+In its original form,Outer Surface Protein B has 12 Beta sheets. However, a  <scene name='G04SecL04Tpc1/Osp_b_fab_complex/1'>truncated form of Osp-B</scene>, purple, is displayed in the complex formed when the C-terminus of Osp B binds to the antibody H6831. The Osp B binds to the Fab <scene name='G04SecL04Tpc1/L_chain/1'> light chain</scene> and <scene name='G04SecL04Tpc1/H_chain/1'>heavy chain</scene>regions of the H6831.
-There are three loop regions on the c-terminal Osp-B that interact with the Fab of H6831. The major interactions of the complex occur between loop region two and the Fab heavy chain.  More minor hydrogen bonding interactions occur between loop one and the heavy chain as well as loop three and the light chains
+There are <scene name='G04SecL04Tpc1/Osp_b_fab_complex/8'>three loop regions</scene> on the c-terminal Osp-B that interact with the Fab of H6831. The major interactions of the complex occur between loop region two, seen in pink, and the Fab heavy chain.  More minor hydrogen bonding interactions occur between loop one,green, and the heavy chain as well as loop three,orange, and the light chains
 <ref name="Becker M">PMID:15713683</ref>. The essential residue on loop two is the <scene name='G04SecL04Tpc1/Osp_b_fab_complex/6'>Lysine 253</scene>shown in green. This lysine forms an ion pair with a <scene name='G04SecL04Tpc1/Osp_b_fab_complex/4'>Glutamic acid 50</scene>, red, of the Fab heavy chain. This antigen-antibody complex is further stabilized by the presence of a <scene name='G04SecL04Tpc1/Osp_b_fab_complex/5'>Threonine 276</scene>, orange. This bond is locked in by the presence of two
 <scene name='G04SecL04Tpc1/Osp_b_fab_complex/7'>aromatic residues</scene> that reside on the Fab, tryptophan and tyrosine shown in black.  There are some instances in which the H6831 cannot bind to Osp-B. This is a case of a mutant form of the protein in which the essential lysine is replaced by another residue<ref name="Becker M">PMID:15713683</ref>.
@@ Line 23: / Line 23: @@
 <Structure load='1FJ1' size='300' frame='true' align='right' caption='OspA and LA2 bound complex' scene='G04SecL04Tpc1/Ospa/1' />
-Another surface protein of note in the B. Burgdorferi is <scene name='G04SecL04Tpc1/Ospa_complex/1'>OspA</scene>, which is 53% similar to OspB. This is due to some structural similarities in the proteins. ***More contents will be done before noon.***
+Another surface protein of note in the B. Burgdorferi is outer surface protein A <scene name='G04SecL04Tpc1/Ospa_complex/1'>OspA</scene>. It is composed of 21 anti-parallel beta-sheets and one alpha-helix.  It contains a B-cell epitope on its C-terminal that binds with monoclonal antibody LA-2.  LA-2 is a regular-structured antibody that is composed of two heavy chains and two light chains. <ref name="Ding,W">PMID: 11183781</ref>.
+Complex proteins OspB and OspA are shown to be 53% similar due to structural similarities<ref name="Li,H">PMID: 9108020</ref>.  The H6831 and LA-2 antibodies are also structurally similar, and each binds near the C-terminus on its respective surface protein.  The H6831 and LA-2 epitopes on OspB and OspA are positioned at the opposite end of the molecule as the N-terminus of each antigen.  On the C-terminal tips on each protein, the epitopes contain three exposed loops of residues that are involved with the binding interaction between antigen and antibody.  For OspB, the middle loop (loop 2) has been shown to have the strongest interaction with H6831. The residue Lys253 in this loop is especially important in the interaction.  For OspA, one of the outer loops (loop 1) has the strongest interaction with LA-2. The <scene name='G04SecL04Tpc1/Ospa_complex/6'>Alanine 208</scene> residue in the loop plays the important role here.  The importance of these residues is confirmed by observing antibody reactivity using different species of Borrelia<ref name="Ding,W">PMID: 11183781</ref><ref name="Li,H">PMID: 9108020</ref>. Also, researchers found that buried surface area of OspA in LA-2 Fab is larger than OspB in the H6831Fab<ref name="Becker M">PMID:15713683</ref>).